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Protein

Phenoloxidase subunit 2

Gene
N/A
Organism
Bombyx mori (Silk moth)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone.

Catalytic activityi

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.
L-tyrosine + O2 = dopaquinone + H2O.

Cofactori

Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi213Copper ABy similarity1
Metal bindingi217Copper ABy similarity1
Metal bindingi243Copper ABy similarity1
Metal bindingi366Copper BBy similarity1
Metal bindingi370Copper BBy similarity1
Metal bindingi406Copper BBy similarity1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • monophenol monooxygenase activity Source: UniProtKB

GO - Biological processi

  • defense response Source: UniProtKB
  • melanin biosynthetic process from tyrosine Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phenoloxidase subunit 2 (EC:1.14.18.1)
Alternative name(s):
PO 2
Tyrosinase 2
OrganismiBombyx mori (Silk moth)Imported
Taxonomic identifieri7091 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
Proteomesi
  • UP000005204 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000359011 – 511 PublicationAdd BLAST51
ChainiPRO_000003590252 – 693Phenoloxidase subunit 2Add BLAST642

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi26N-linked (GlcNAc...)Sequence analysis1
Glycosylationi64N-linked (GlcNAc...)Sequence analysis1
Glycosylationi462N-linked (GlcNAc...)Sequence analysis1
Glycosylationi494N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi583 ↔ 627By similarity
Disulfide bondi585 ↔ 634By similarity
Glycosylationi680N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

The N-terminus is blocked.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Tissue specificityi

Synthesized by hemocytes and released into the hemolymph plasma.1 Publication

Interactioni

Subunit structurei

Heterodimer.1 Publication

Protein-protein interaction databases

STRINGi7091.BGIBMGA013115-TA.

Structurei

3D structure databases

ProteinModelPortaliQ27452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Phylogenomic databases

eggNOGiENOG410IY2J. Eukaryota.
ENOG4111KTW. LUCA.
InParanoidiQ27452.
OMAiTTVRIFI.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSiPR00187. HAEMOCYANIN.
SUPFAMiSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q27452-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADVFESLEL LFDRPNEPLI TPKGENNSVF QLTEQFLTED YANNGIELNN
60 70 80 90 100
RFGDDASEKI PLKNLSKLPE FKIATQLPKD AEFSLFLPKH QEMANELLGV
110 120 130 140 150
LMDVPENELQ DLLSTCAFAR VNLNPQLFNY CYSVALMHRR DTRKVRVKNF
160 170 180 190 200
AEVFPSKFLD SQVFTQARET AAVIPPDVPR IPIIIPRDYT ATDLEEEHRL
210 220 230 240 250
AYWREDIGIN LHHYHWHLVY PFTANDLSIV AKDRRGELFF YMHQQVIARF
260 270 280 290 300
NCERLCNSLK RVKKFSNWRE PIPEAYFPKL DSLTSSRGWP PRQSGMQWQD
310 320 330 340 350
LNRAAEGLFV TIDEMERWRR NVEEAIATGT VRLPNGQTRP LDIDTLGNML
360 370 380 390 400
ESSALSPNRE LYGSIHNNGH SFTAYMHDPE HRYLEQFGVI ADEATTMRDP
410 420 430 440 450
FFYRWHAYID DVFQKHKESA YVRPYTRSEL ENPGVQVRSV SVETPGGQPN
460 470 480 490 500
TLNTFWMLSD VNLSRGLDFS DNGPVYARFT HLNYRHFSYR INVNNTGSSR
510 520 530 540 550
RTTVRIFITP KFDERNVPWI FSDQRKMCIE MDRFVTVLNA GENNIVRQST
560 570 580 590 600
ESSITIPFEQ TFRDLSAQGN DPRRDELATF NYCGCGWPQH MLVPKGTEAG
610 620 630 640 650
MPFQLFVMLS NYDLDRIDQD DGKQLTCVEA SSFCGLKDKK YPDRRAMGFP
660 670 680 690
FDRPSSSATS LQDFILPNMG LQDITIQLQN VTEPNPRNPP MSV
Length:693
Mass (Da):80,119
Last modified:January 1, 1999 - v2
Checksum:i013114DF4CC1A926
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti433P → Q AA sequence (PubMed:7644494).Curated1

Mass spectrometryi

Molecular mass is 81105 Da from positions 52 - 693. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49371 mRNA. Translation: BAA08369.1.
AB048762 mRNA. Translation: BAB41101.1.
RefSeqiNP_001037534.1. NM_001044069.1.
UniGeneiBmo.10373.
Bmo.1389.

Genome annotation databases

EnsemblMetazoaiBGIBMGA013115-RA; BGIBMGA013115-TA; BGIBMGA013115.
GeneIDi693073.
KEGGibmor:693073.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49371 mRNA. Translation: BAA08369.1.
AB048762 mRNA. Translation: BAB41101.1.
RefSeqiNP_001037534.1. NM_001044069.1.
UniGeneiBmo.10373.
Bmo.1389.

3D structure databases

ProteinModelPortaliQ27452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7091.BGIBMGA013115-TA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiBGIBMGA013115-RA; BGIBMGA013115-TA; BGIBMGA013115.
GeneIDi693073.
KEGGibmor:693073.

Organism-specific databases

CTDi35910.

Phylogenomic databases

eggNOGiENOG410IY2J. Eukaryota.
ENOG4111KTW. LUCA.
InParanoidiQ27452.
OMAiTTVRIFI.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSiPR00187. HAEMOCYANIN.
SUPFAMiSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRP2_BOMMO
AccessioniPrimary (citable) accession number: Q27452
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 1, 1999
Last modified: September 7, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.